ArticleContrast media & molecular imaging
Kinetic analysis of hyaluronidase activity using a bioactive MRI contrast agent.
Article in Contrast media & molecular imaging. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Inflammatory microenvironment-responsive MR imaging contrast agents.Nanomedicine (London, England) · 2025Review
- MRI Contrast Agents in Glycobiology.Molecules (Basel, Switzerland) · 2022Review
- The Labeling, Visualization, and Quantification of Hyaluronan Distribution in Tumor-Bearing Mouse Using PET and MR Imaging.Pharmaceutical research · 2020Article
- Chemistry of MRI Contrast Agents: Current Challenges and New Frontiers.Chemical reviews · 2019Review
- Detecting enzyme activities with exogenous MRI contrast agents.Chemistry (Weinheim an der Bergstrasse, Germany) · 2014Review
- Imaging aspects of the tumor stroma with therapeutic implications.Pharmacology & therapeutics · 2014Review
- Emerging roles for hyaluronidase in cancer metastasis and therapy.Advances in cancer research · 2014Review
- Molecular imaging and targeted therapies.Biochemical pharmacology · 2010Review
- Peritoneal adhesion and angiogenesis in ovarian carcinoma are inversely regulated by hyaluronan: the role of gonadotropins.Neoplasia (New York, N.Y.) · 2010Article
- Hyaluronidase activity of human Hyal1 requires active site acidic and tyrosine residues.The Journal of biological chemistry · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
One of the attractions of molecular imaging using 'smart' bioactive contrast agents is the ability to provide non-invasive data on the spatial and temporal changes in the distribution and expression patterns of specific enzymes. The tools developed for that aim could potentially also be developed for functional imaging of enzyme activity itself, through quantitative analysis of the rapid dynamics of enzymatic conversion of these contrast agents. High molecular weight hyaluronan, the natural substrate of hyaluronidase, is a major antiangiogenic constituent of the extracellular matrix. Degradation by hyaluronidase yields low molecular weight fragments, which are proangiogenic. A novel contrast material, HA-GdDTPA-beads, was designed to provide a substrate analog of hyaluronidase in which relaxivity changes are induced by enzymatic degradation. We show here a first-order kinetic analysis of the time-dependent increase in R(2) as a result of hyaluronidase activity. The changes in R(2) and the measured relaxivity of intact HA-GdDTPA-beads (r(2B)) and HA-GdDTPA fragments (r(2D)) were utilized for derivation of the temporal drop in concentration of GdDTPA in HA-GdDTPA-beads as the consequence of the release of HA-GdDTPA fragments. The rate of dissociation of HA-GdDTPA from the beads showed typical bell-shaped temperature dependence between 7 and 36 degrees C with peak activity at 25 degrees C. The tools developed here for quantitative dynamic analysis of hyaluronidase activity by MRI would allow the use of activation of HA-GdDTPA-beads for the determination of the role of hyaluronidase in altering the angiogenic microenvironment of tumor micro metastases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.